Quantitative Benchmarking of Catalytic Parameters for Enzyme-Mimetic Ribonucleotide Dephosphorylation by Iron Oxide Minerals

氧化铁矿物催化模拟核糖核苷酸脱磷酸化反应的催化参数定量基准测试

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Abstract

Iron oxides, which are documented phosphorus (P) sinks as adsorbents, have been shown to catalyze organic P dephosphorylation, implicating these minerals as catalytic traps in P cycling. However, quantitative evaluation of this abiotic catalysis is lacking. Here, we investigated the dephosphorylation kinetics of eight ribonucleotides, with different nucleobase structures and P stoichiometry, reacting with common iron oxides. X-ray absorption spectroscopy determined that 0-98% of mineral-bound P was recycled inorganic P (P(i)). Matrix-assisted laser desorption/ionization with mass spectrometry demonstrated short-lived triphosphorylated and monophosphorylated ribonucleotides bound to goethite. Based on Michaelis-Menten type modeling of the kinetic evolution of both dissolved and mineral-bound P(i), maximal P(i) production rates from triphosphorylated ribonucleotides reacted with goethite (1.9-16.1 μmol P(i) h(-1) g(goethite)(-1)) were >5-fold higher than with hematite and ferrihydrite; monophosphorylated ribonucleotides generated only mineral-bound P(i) at similar rates (0.0-12.9 μmol P(i) h(-1) g(mineral)(-1)) across minerals. No clear distinction was observed between purine-based and pyrimidine-based ribonucleotides. After normalization to mineral-dependent P(i) binding capacity, resulting catalytic turnover rates implied surface chemistry-controlled reactivity. Ribonucleotide-mineral complexation mechanisms were identified with infrared spectroscopy and molecular modeling. We estimated iron oxide-catalyzed rates in soil (0.01-5.5 μmol P(i) h(-1) g(soil)) comparable to reported soil phosphatase rates, highlighting both minerals and enzymes as relevant catalysts in P cycling.

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